Protein Family Models

This entry represents a dCTP deaminase (DCD) domain found in archaea and bacteria [1-5]. Methanococcus jannaschii, has a bifunctional enzyme DCD-DUT, that harbors both dCTP deaminase and dUTP pyrophosphatase activities [1]. Paper describing PDB structure 1ogh. [1]. 12756253. Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases. Johansson E, Bjornberg O, Nyman PO, Larsen S;. J Biol Chem. 2003;278:27916-27922. Paper describing PDB structure 1xs1. [2]. 15539408. Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes. Johansson E, Fano M, Bynck JH, Neuhard J, Larsen S, Sigurskjold BW, Christensen U, Willemoes M;. J Biol Chem. 2005;280:3051-3059. Paper describing PDB structure 2j4h. [3]. 17651436. Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme. Johansson E, Thymark M, Bynck JH, Fano M, Larsen S, Willemoes M;. FEBS J. 2007;274:4188-4198. Paper describing PDB structure 2qlp. [4]. 18164314. Mechanism of dTTP inhibition of the bifunctional dCTP deaminase:dUTPase encoded by Mycobacterium tuberculosis. Helt SS, Thymark M, Harris P, Aagaard C, Dietrich J, Larsen S, Willemoes M;. J Mol Biol. 2008;376:554-569. Paper describing PDB structure 2v9x. [5]. 17996716. Mutational analysis of the nucleotide binding site of Escherichia coli dCTP deaminase. Thymark M, Johansson E, Larsen S, Willemoes M;. Arch Biochem Biophys. 2008;470:20-26. (from Pfam)

Date:

2024-10-16

This entry includes several bacterial 2'-deoxycytidine 5'-triphosphate deaminase proteins (EC:3.5.4.13) (DCD) which consist of two dUTPase-like domains (PDBe:2r9q). This entry represents the N-terminal catalytic domain, which contains the active site residues Arg115 and Glu138, important for its activity [1]. [1]. 15539408. Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes. Johansson E, Fano M, Bynck JH, Neuhard J, Larsen S, Sigurskjold BW, Christensen U, Willemoes M;. J Biol Chem. 2005;280:3051-3059. (from Pfam)

Date:

2024-10-16

dCTP deaminase catalyzes the formation of dUTP from dCTP

Date:

2023-03-07

Members of this family include the Escherichia coli monofunctional deoxycytidine triphosphate deaminase (dCTP deaminase) and a Methanocaldococcus jannaschii bifunctional dCTP deaminase (3.5.4.13)/dUTP diphosphatase (EC 3.6.1.23), which has the EC number 3.5.4.30 for the overall operation.

Gene:

dcd

Date:

2024-05-29